SAXSdb — 2cqx

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1. Protein Identity and Related Structures Protein Identity & Related Structures

LAG1 longevity assurance homolog 5

Mus musculus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 77–135	Fragment：residues 8-66	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 120mM NaCl；Pressure ambient NMR sample composition：1.30mM Domain U 15N, 13C; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2CQX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5E8N The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b) Deposited 2015-10-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 379–387（9 aa） Fragment：UNP residues 379-387	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.9 M Ammonium sulphate, 0.1 M Tris-HCl	Resolution 2.25 Å R-free 0.286
5E8N The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b) Deposited 2015-10-14	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 379–387（9 aa） Fragment：UNP residues 379-387	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.9 M Ammonium sulphate, 0.1 M Tris-HCl	Resolution 2.25 Å R-free 0.286
5E8N The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b) Deposited 2015-10-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 379–387（9 aa） Fragment：UNP residues 379-387	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.9 M Ammonium sulphate, 0.1 M Tris-HCl	Resolution 2.25 Å R-free 0.286
5E8N The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b) Deposited 2015-10-14	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 379–387（9 aa） Fragment：UNP residues 379-387	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.9 M Ammonium sulphate, 0.1 M Tris-HCl	Resolution 2.25 Å R-free 0.286
5E8O The structure of the TEIPP associated altered peptide ligand Trh4-p2ABU in complex with H-2D(b) Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 379–387（9 aa） Fragment：UNP residues 379-387	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；1.5 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl	Resolution 1.98 Å R-free 0.254
5E8O The structure of the TEIPP associated altered peptide ligand Trh4-p2ABU in complex with H-2D(b) Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 379–387（9 aa） Fragment：UNP residues 379-387	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；1.5 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl	Resolution 1.98 Å R-free 0.254
5E8P The structure of the TEIPP associated altered peptide ligand Trh4-p5NLE in complex with H-2D(b) Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 379–387（9 aa） Fragment：UNP residues 379-387	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl	Resolution 2.00 Å R-free 0.258
5E8P The structure of the TEIPP associated altered peptide ligand Trh4-p5NLE in complex with H-2D(b) Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 379–387（9 aa） Fragment：UNP residues 379-387	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl	Resolution 2.00 Å R-free 0.258

3 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LASS5_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–66； UniProt 77–135

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2cqx
Deposition date deposition_date	2005-05-20
Structure title title	Solution structure of RSGI RUH-034, a homeodomain from mouse cDNA
Keywords keywords	;Homeodomain, DNA binding domain, Transcription, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, UNKNOWN FUNCTION ;; STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	14.88 Å
Radius of gyration Rg (electron density) rg_electron	14.42 Å
Forward intensity I(0) i0	393292000.00
Molecular weight molecular_weight	160400.0 kDa
Excluded volume excluded_volume	198820 Å³
Envelope volume envelope_volume	42989 Å³
Hydration-shell volume shell_volume	18217 Å³
Envelope diameter envelope_diameter	71.8 Å
Shell Rg shell_rg	26.48 Å
Envelope Rg envelope_rg	21.66 Å
Shape Rg shape_rg	14.35 Å
Total Rg total_rg	15.04 Å
Total atoms total_atoms	22640
Residues n_residues	1440
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	40.1 Å
Rg (real space) rg_real	13.98 Å
Rg uncertainty (real space) rg_real_error	0.07 Å
I(0) (real space) i0_real	3.7480e+08
I(0) uncertainty (real space) i0_real_error	3.1940e+06
Rg (reciprocal space) rg_reciprocal	15.08 Å
I(0) (reciprocal space) i0_reciprocal	393300000.0000
Solution quality estimate total_estimate	0.6569
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.395
Kurtosis Kurtosis kurtosis	-0.319
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	4.0040
Highest regularization parameter α highest_alpha	245700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.008; Oscil: 0.865; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2cqxa1
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.1 — Homeodomain-like
Family Family family	a.4.1.1 — Homeodomain

Domain ID domain_id	d2cqxa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2cqxa3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	2cqxA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	60 — Homeodomain-like

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8. Citations (1)

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Description description	LAG1 longevity assurance homolog 5
Molecular weight formula_weight	8046.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	22640

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090

fit	/app/data/saxs_computation/cq/2cqx/2cqx.fit
pddf	/app/data/pr_computation/cq/2cqx/2cqx.pr.out
profile	/app/data/saxs_computation/cq/2cqx/2cqx.dat

Solution structure of RSGI RUH-034, a homeodomain from mouse cDNA

1. Protein Identity and Related Structures Protein Identity & Related Structures

LAG1 longevity assurance homolog 5

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)